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Regularized Speaker Adaptation of KL-HMM for Dysarthric Speech Recognition
Myungjong Kim,Younggwan Kim,Joohong Yoo,Jun Wang,Hoirin Kim IEEE 2017 IEEE transactions on neural systems and rehabilita Vol.25 No.9
<P>This paper addresses the problem of recognizing the speech uttered by patients with dysarthria, which is a motor speech disorder impeding the physical production of speech. Patients with dysarthria have articulatory limitation, and therefore, they often have trouble in pronouncing certain sounds, resulting in undesirable phonetic variation. Modern automatic speech recognition systems designed for regular speakers are ineffective for dysarthric sufferers due to the phonetic variation. To capture the phonetic variation, Kullback-Leibler divergence-based hidden Markov model (KL-HMM) is adopted, where the emission probability of state is parameterized by a categorical distribution using phoneme posterior probabilities obtained from a deep neural network-based acoustic model. To further reflect speaker-specific phonetic variation patterns, a speaker adaptation method based on a combination of L2 regularization and confusion-reducing regularization, which can enhance discriminability between categorical distributions of the KL-HMM states while preserving speaker-specific information is proposed. Evaluation of the proposed speaker adaptation method on a database of several hundred words for 30 speakers consisting of 12 mildly dysarthric, 8 moderately dysarthric, and 10 non-dysarthric control speakers showed that the proposed approach significantly outperformed the conventional deep neural network-based speaker adapted system on dysarthric as well as non-dysarthric speech.</P>
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Lee, Wonhae,Kim, Ki Ra,Singaravelu, Gunasekaran,Park, Byung-Jae,Kim, Do Han,Ahnn, Joohong,Yoo, Yung Joon WILEY-VCH 2006 Proteomics Vol. No.
<P>Proper folding and maintenance of the native structure are central to protein function and are assisted by a family of proteins called chaperones. Calreticulin and calnexin are ER resident chaperones well conserved from worm to human. Calreticulin/calnexin knock-out mice exhibit a severe phenotype, whereas in Caenorhabditis elegans, calreticulin [crt-1(jh101)]- and calnexin [cnx-1(nr2009)]-null mutant worms exhibit only a mild phenotype, suggesting the possible existence of alternative chaperone machinery that can compensate for the deficiency of calreticulin and/or calnexin. In order to rapidly identify the compensatory chaperone components involved in this process, we analyzed the proteome of crt-1(jh101) mutants and [crt-1(jh101);cnx-1(nr2009)] double mutants. When grown at 20°C, we found that five proteins were up-regulated and two proteins were down-regulated in crt-1(jh101) mutants; nine proteins were up-regulated and five proteins were down-regulated in [crt-1(jh101);cnx-1(nr2009)] double mutants. In addition, elevation of the cultivation temperature to 25°C, which is still permissive to growth but causes specific defects in mutants, led to the identification of several additional proteins. Interestingly, the consistent increment of heat shock protein-70 family members (hsp70) together with protein disulfide isomerase (PDI) at all the examined conditions suggests the possible compensatory function imparted by hsp70 and PDI family members in the absence of calreticulin and/or calnexin.</P>
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